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Q9U8B8

- DYR_HELVI

UniProt

Q9U8B8 - DYR_HELVI

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Protein
Dihydrofolate reductase
Gene
DHFR
Organism
Heliothis virescens (Tobacco budworm moth)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.By similarity

Enzyme regulationi

Activated by dithiothreitol and p-chloromercuribenzoate. Inhibited by trimethoprim, methotrexate, sodium tetrathionate and hydroxymercuribenzoate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei71 – 711Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 237NADP By similarity
Nucleotide bindingi55 – 573NADP By similarity
Nucleotide bindingi77 – 793NADP By similarity
Nucleotide bindingi117 – 1248NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. dihydrofolate reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:DHFR
OrganismiHeliothis virescens (Tobacco budworm moth)
Taxonomic identifieri7102 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeHeliothinaeHeliothis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Dihydrofolate reductase
PRO_0000186371Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9U8B8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 184180DHFR
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 366Substrate binding By similarity

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.By similarity

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9U8B8-1 [UniParc]FASTAAdd to Basket

« Hide

MSQVKLNLIA AACDNMGIGV NGALPWRLKK EMAYFTTMTS KVSEPTKVNA    50
VIMGRRTWDC IPDKYRPLQD RVNIVLTHNV DSVKENVPEG VMVFPGLDEA 100
IKYIEGREDI ESTWVIGGSS IYRAAMTHPN CGKIYLTEIQ KSFDCDTFFP 150
NIDKQQFHLV DEEQIPGEKQ VEGNISYYFR VYKKL 185
Length:185
Mass (Da):21,089
Last modified:May 1, 2000 - v1
Checksum:i9B8C0E50ED175812
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → L AA sequence 1 Publication
Sequence conflicti7 – 71N → D AA sequence 1 Publication
Sequence conflicti11 – 133AAC → IFD AA sequence 1 Publication
Sequence conflicti15 – 151N → D AA sequence 1 Publication
Sequence conflicti21 – 211N → D AA sequence 1 Publication
Sequence conflicti158 – 1581H → Q AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104106 mRNA. Translation: AAF04459.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104106 mRNA. Translation: AAF04459.1 .

3D structure databases

ProteinModelPortali Q9U8B8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Tobacco budworm dihydrofolate reductase is a promising target for insecticide discovery."
    Walker V.K., Tyshenko M.G., Kuiper M.J., Dargar R.V., Yuhas D.A., Cruickshank P.A., Chaguturu R.
    Eur. J. Biochem. 267:394-403(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-22; 32-38; 143-149; 153-159 AND 170-175, ENZYME REGULATION.
    Tissue: Larva.

Entry informationi

Entry nameiDYR_HELVI
AccessioniPrimary (citable) accession number: Q9U8B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 2000
Last modified: October 16, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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